High-Intensity Ultrasound Modified the Functional Properties of Neosalanx Taihuensis Myofibrillar Protein and Improved its Emulsion Stability

Abstract

This study aimed to investigate the effects of high-intensity ultrasound treatment  on the functional properties and emulsion stability of Neosalanx taihuensis myofibrillar protein (MP). The results showed that the carbonyl groups, emulsification properties, intrinsic fluorescence intensity, and surface hydrophobicity of the ultrasound treated MP solution were increased compared to the MP without ultrasound treatment. The results of secondary structure showed that the ultrasound treatment could cause a huge rise increase of β-sheet and a decline of α-helix of MP, indicating that ultrasound induced molecular unfolding and stretching. Moreover, ultrasound reduced the content of total sulfhydryl and led to a certain degree of MP cross-linking. The microscopic morphology of MP emulsion indicated that the emulsion droplet decreased with the increase of ultrasound power. In addition, ultrasound could also reduce the apparent viscosity of the MP emulsion and increased storage modulus. The results for the lipid oxidation products indicated that ultrasound significantly improved the oxidative stability of N. taihuensis MP emulsions. This study offers an important reference theoretically for the ultrasound modification of aquatic proteins and the future development of N. taihuensis deep-processed products represented by surimi.

Keywords: Neosalanx taihuensis, Ultrasound, Myofibrillar protein, Functional properties, Emulsion stability